6ds5 | pdb_00006ds5

Cryo EM structure of human SEIPIN

spinqualitylabelsall models 6ds5, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ds5 is a 11 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Gene: BSCL2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [BSCL2_HUMAN] Autosomal dominant spastic paraplegia type 17;Severe neurodegenerative syndrome with lipodystrophy;Distal hereditary motor neuropathy type 5;Berardinelli-Seip congenital lipodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function [BSCL2_HUMAN] Is a regulator of lipid catabolism essential for adipocyte differentiation. May also be involved in the central regulation of energy homeostasis (By similarity). Necessary for correct lipid storage and lipid droplets maintenance; may play a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues. Publication Abstract from PubMed The biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a critical role in both LD formation and adipogenesis. The molecular function of SEIPIN, however, has yet to be elucidated. Here, we report the cryogenic electron microscopy structure of human SEIPIN at 3.8 A resolution. SEIPIN exists as an undecamer, and this oligomerization state is critical for its physiological function. The evolutionarily conserved lumenal domain of SEIPIN forms an eight-stranded beta sandwich fold. Both full-length SEIPIN and its lumenal domain can bind anionic phospholipids including phosphatidic acid. Our results suggest that SEIPIN forms a scaffold that helps maintain phospholipid homeostasis and surface tension of the ER. Human SEIPIN Binds Anionic Phospholipids.,Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H Dev Cell. 2018 Oct 22;47(2):248-256.e4. doi: 10.1016/j.devcel.2018.09.010. Epub, 2018 Oct 4. PMID:30293840 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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